Manganese in PDB 1szx: Role of Hydrogen Bonding in the Active Site of Human Manganese Superoxide Dismutase

All present enzymatic activity of Role of Hydrogen Bonding in the Active Site of Human Manganese Superoxide Dismutase:
1.15.1.1;

The structure of Role of Hydrogen Bonding in the Active Site of Human Manganese Superoxide Dismutase, PDB code: 1szx was solved by W.B.Greenleaf, J.J.Perry, A.S.Hearn, D.E.Cabelli, J.R.Lepock, M.E.Stroupe, J.A.Tainer, H.S.Nick, D.N.Silverman, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 1.95
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	73.947, 75.601, 68.437, 90.00, 90.00, 90.00
R / Rfree (%)	24.2 / 29

The binding sites of Manganese atom in the Role of Hydrogen Bonding in the Active Site of Human Manganese Superoxide Dismutase (pdb code 1szx). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Role of Hydrogen Bonding in the Active Site of Human Manganese Superoxide Dismutase, PDB code: 1szx:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the Role of Hydrogen Bonding in the Active Site of Human Manganese Superoxide Dismutase


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Role of Hydrogen Bonding in the Active Site of Human Manganese Superoxide Dismutase within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn199 b:33.2 occ:1.00 OD1 A:ASP159 2.1 31.7 1.0 O A:HOH394 2.1 37.0 1.0 NE2 A:HIS163 2.1 29.8 1.0 NE2 A:HIS74 2.2 35.8 1.0 NE2 A:HIS26 2.2 34.5 1.0 CE1 A:HIS163 3.0 26.2 1.0 CE1 A:HIS26 3.1 31.0 1.0 CE1 A:HIS74 3.1 34.4 1.0 CG A:ASP159 3.1 30.6 1.0 CD2 A:HIS163 3.3 28.9 1.0 CD2 A:HIS26 3.3 32.0 1.0 CD2 A:HIS74 3.3 34.1 1.0 OD2 A:ASP159 3.4 28.9 1.0 ND1 A:HIS163 4.2 26.3 1.0 ND1 A:HIS26 4.2 30.8 1.0 ND1 A:HIS74 4.2 34.8 1.0 CG A:HIS26 4.3 32.4 1.0 CG A:HIS163 4.3 28.8 1.0 CG A:HIS74 4.3 34.2 1.0 CB A:ASP159 4.4 29.0 1.0 CB A:TRP161 4.5 30.1 1.0 NE2 A:GLN143 4.6 32.1 1.0 CZ A:PHE123 4.6 30.4 1.0 CG A:TRP161 4.6 31.0 1.0 CD1 A:TRP161 4.8 29.1 1.0 CE1 A:PHE123 4.9 31.0 1.0

Manganese binding site 2 out of 2 in the Role of Hydrogen Bonding in the Active Site of Human Manganese Superoxide Dismutase


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Role of Hydrogen Bonding in the Active Site of Human Manganese Superoxide Dismutase within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn199 b:27.0 occ:1.00 OD1 B:ASP159 2.1 25.7 1.0 O B:HOH422 2.1 33.4 1.0 NE2 B:HIS163 2.2 17.8 1.0 NE2 B:HIS26 2.2 32.0 1.0 NE2 B:HIS74 2.2 29.9 1.0 CD2 B:HIS163 3.0 21.7 1.0 CG B:ASP159 3.1 22.7 1.0 CE1 B:HIS74 3.1 29.1 1.0 CD2 B:HIS26 3.2 31.1 1.0 CE1 B:HIS26 3.2 31.6 1.0 CE1 B:HIS163 3.2 25.4 1.0 CD2 B:HIS74 3.3 29.2 1.0 OD2 B:ASP159 3.4 21.2 1.0 CG B:HIS163 4.2 23.4 1.0 ND1 B:HIS163 4.3 21.7 1.0 ND1 B:HIS74 4.3 27.8 1.0 ND1 B:HIS26 4.3 30.1 1.0 CG B:HIS26 4.3 30.1 1.0 CG B:HIS74 4.4 28.2 1.0 CB B:ASP159 4.4 22.9 1.0 CB B:TRP161 4.5 25.5 1.0 NE2 B:GLN143 4.6 31.3 1.0 CG B:TRP161 4.7 26.6 1.0 O B:HOH309 4.7 33.5 1.0 CZ B:PHE123 4.7 25.6 1.0 CD1 B:TRP161 4.9 23.0 1.0 CB B:ALA164 5.0 30.1 1.0 CE1 B:PHE123 5.0 26.1 1.0

W.B.Greenleaf, J.J.Perry, A.S.Hearn, D.E.Cabelli, J.R.Lepock, M.E.Stroupe, J.A.Tainer, H.S.Nick, D.N.Silverman. Role of Hydrogen Bonding in the Active Site of Human Manganese Superoxide Dismutase. Biochemistry V. 43 7038 2004.
ISSN: ISSN 0006-2960
PubMed: 15170341
DOI: 10.1021/BI049888K